| First Author | Collins RE | Year | 2008 |
| Journal | Nat Struct Mol Biol | Volume | 15 |
| Issue | 3 | Pages | 245-50 |
| PubMed ID | 18264113 | Mgi Jnum | J:382259 |
| Mgi Id | MGI:8310517 | Doi | 10.1038/nsmb.1384 |
| Citation | Collins RE, et al. (2008) The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat Struct Mol Biol 15(3):245-50 |
| abstractText | Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark. |
